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PYK2 pyruvate kinase PYK2 [ Saccharomyces cerevisiae S288C ]

Gene ID: 854529, updated on 17-May-2024

Summary

Gene symbol
PYK2
Gene description
pyruvate kinase PYK2
Primary source
FungiDB:YOR347C
Locus tag
YOR347C
See related
SGD:S000005874; AllianceGenome:SGD:S000005874
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables melatonin binding activity and pyruvate kinase activity. Involved in pyruvate metabolic process. Located in mitochondrion. Human ortholog(s) of this gene implicated in Gaucher's disease; congenital nonspherocytic hemolytic anemia; malaria; pyruvate kinase deficiency of red cells; and type 2 diabetes mellitus. Orthologous to human PKLR (pyruvate kinase L/R) and PKM (pyruvate kinase M1/2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

See PYK2 in Genome Data Viewer
Location:
chromosome: XV
Exon count:
1
Sequence:
Chromosome: XV; NC_001147.6 (984942..986462, complement)

Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene tRNA-Pro Neighboring gene deoxycytidyl transferase Neighboring gene proline permease PUT4 Neighboring gene Cin1p

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
 
enables kinase activity IEA
Inferred from Electronic Annotation
more info
 
enables magnesium ion binding IEA
Inferred from Electronic Annotation
more info
 
enables melatonin binding IDA
Inferred from Direct Assay
more info
PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
 
enables potassium ion binding IEA
Inferred from Electronic Annotation
more info
 
enables pyruvate kinase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables pyruvate kinase activity IEA
Inferred from Electronic Annotation
more info
 
enables pyruvate kinase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
Process Evidence Code Pubs
involved_in glycolytic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in glycolytic process IEA
Inferred from Electronic Annotation
more info
 
involved_in monocarboxylic acid metabolic process IEA
Inferred from Electronic Annotation
more info
 
involved_in pyruvate metabolic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in mitochondrion IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
pyruvate kinase PYK2
NP_014992.3
  • Pyruvate kinase; appears to be modulated by phosphorylation; transcription repressed by glucose, and Pyk2p may be active under low glycolytic flux; PYK2 has a paralog, CDC19, that arose from the whole genome duplication

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001147.6 Reference assembly

    Range
    984942..986462 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183767.3NP_014992.3  TPA: pyruvate kinase PYK2 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_014992.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W342, P52489
    UniProtKB/TrEMBL
    A0A6A5Q8H1, A6ZPH7, B3LK04, B5VSM3, C7GNS1, C8ZH98, G2WNK7, N1P3V3
    Conserved Domains (1) summary
    cd00288
    Location:20502
    Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...